Proteostatic Hotspots in Amyloid Fibrils Protect Us from Neurodegeneration
Author:
Publisher
Elsevier BV
Subject
Developmental Biology,Cell Biology,General Biochemistry, Genetics and Molecular Biology,Molecular Biology
Reference10 articles.
1. Adapting Proteostasis for Disease Intervention
2. A molecular chaperone breaks the catalytic cycle that generates toxic Aβ oligomers
3. Functional amyloid – from bacteria to humans
4. Comparing protein folding in vitro and in vivo: foldability meets the fitness challenge
5. The BRICHOS Domain, Amyloid Fibril Formation, and Their Relationship
Cited by 5 articles. 订阅此论文施引文献 订阅此论文施引文献，注册后可以免费订阅5篇论文的施引文献，订阅后可以查看论文全部施引文献
1. Identification of potential aggregation hotspots on Aβ42 fibrils blocked by the anti-amyloid chaperone-like BRICHOS domain;Nature Communications;2024-02-01
2. Bri2 BRICHOS client specificity and chaperone activity are governed by assembly state;Nature Communications;2017-12
3. Dementia-related Bri2 BRICHOS is a versatile molecular chaperone that efficiently inhibits Aβ42 toxicity in Drosophila;Biochemical Journal;2016-10-11
4. Current and future treatment of amyloid diseases;Journal of Internal Medicine;2016-05-10
5. BRICHOS binds to a designed amyloid-forming β-protein and reduces proteasomal inhibition and aggresome formation;Biochemical Journal;2016-01-05
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